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Q2IMF3 (PROB_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate 5-kinase

EC=2.7.2.11
Alternative name(s):
Gamma-glutamyl kinase
Short name=GK
Gene names
Name:proB
Ordered Locus Names:Adeh_0211
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline By similarity. HAMAP-Rule MF_00456

Catalytic activity

ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP-Rule MF_00456

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP-Rule MF_00456

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00456.

Sequence similarities

Belongs to the glutamate 5-kinase family.

Contains 1 PUA domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: InterPro

glutamate 5-kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000252970

Regions

Domain282 – 36079PUA
Nucleotide binding176 – 1772ATP By similarity

Sites

Binding site151ATP By similarity
Binding site541Substrate By similarity
Binding site1441Substrate By similarity
Binding site1561Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IMF3 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: A160F153C1E1A3BC

FASTA37939,855
        10         20         30         40         50         60 
MSRSALRRVK RLVVKVGTGT LTDRAGRFDR DNCARLASEL AEVSRGRKVV LVSSGAVALG 

        70         80         90        100        110        120 
AERLGLARSR GKPWDLPTKQ ACAAAGQPHL MAAWGEALGR HGLVTAQVLL TADDLASRKR 

       130        140        150        160        170        180 
FLNARRTFER LLDAGAVPVV NENDTVAVDE LKVGDNDTLA ALVAGCVEAD AVAMLTDVDG 

       190        200        210        220        230        240 
LYDRNPAEPG ARLLRDVPRV TAEIERSAGG AGSERSVGGM ITKVKAARRL GAQGVVTALL 

       250        260        270        280        290        300 
SGRRARALPA LLAGEPVGTV FAPGAHRLSS RQGWLAAAAR GKGVILVDAG ARRALVEQGR 

       310        320        330        340        350        360 
SLLPSGVRGV QGQFGVGDPV DVAVDPARPF ARGLAGYAAD EVRRIAGLKT GEIERALGYK 

       370 
YLDEIVHRND LVVLETGRE 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC79988.1.
RefSeqYP_463425.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2IMF3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290397.Adeh_0211.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC79988; ABC79988; Adeh_0211.
GeneID3886293.
KEGGade:Adeh_0211.
PATRIC20916445. VBIAnaDeh31384_0227.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMARLMRAYE.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycADEH290397:GI2Z-213-MONOMER.
UniPathwayUPA00098; UER00359.

Family and domain databases

Gene3D2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPMF_00456. ProB.
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
IPR011529. Glu_5kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR002478. PUA.
IPR015947. PUA-like_domain.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_ANADE
AccessionPrimary (citable) accession number: Q2IMF3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 7, 2006
Last modified: May 14, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways